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Phosphorylation on the PPP2R5D B regulatory sub unit modulates the biochemical properties of protein phosphatase 2A

Title
Phosphorylation on the PPP2R5D B regulatory sub unit modulates the biochemical properties of protein phosphatase 2A
Authors
Yu U.Y.Ahn J.-H.
Ewha Authors
안정혁
SCOPUS Author ID
안정혁scopus
Issue Date
2010
Journal Title
BMB Reports
ISSN
1976-6696JCR Link
Citation
vol. 43, no. 4, pp. 263 - 267
Indexed
SCIE; SCOPUS; KCI WOS scopus
Abstract
To characterize the biochemical properties of the PP2A regulatory B subunit, PPP2R5D, we analyzed its phosphorylation sites, stoichiometry and effect on holoenzyme activity. PPP2R5D was phosphorylated on Ser-53, Ser-68, Ser-81, and Ser-566 by protein kinase A, and mutations at all four of these sites abolished any significant phosphorylation in vitro. In HEK293 cells, however, the Ser-566 was the major phosphorylation site after PKA activation by forskolin, with marginal phosphorylation on Ser-81. Inhibitory tyrosine phosphorylation on Tyr-307 of the PP2A catalytic C subunit was decreased after forskolin treatment. Kinetic analysis showed that overall PP2A activity was increased with phosphorylation by PPP2R5D phosphorylation. The apparent Km was reduced from 11.25 μM to 1.175 μM with PPP2R5D phosphorylation, resulting in an increase in catalytic activity. These data suggest that PKA mediated activation of PP2A is enabled by PPP2R5D phosphorylation, which modulates the affinity of the PP2A holoenzyme to its physiological substrates.
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의학전문대학원 > 의학과 > Journal papers
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